Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 757-761Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109025329
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Funding
- National Natural Science Foundation of China [30870488]
- Ministry of Science and Technology of China [2009CB918800]
- ANR Jeunes Chercheurs 2005 [ANR-05-JCJC-0049-01]
- FPG EUR-INTAFAR [LSHM-CT-2004-512138]
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Spr1274 is a putative choline-binding protein that is bound to the cell wall of Streptococcus pneumoniae through noncovalent interactions with the choline moieties of teichoic and lipoteichoic acids. Its function is still unknown. The crystal structure of the choline-binding domain of Spr1274 (residues 44-129) was solved at 2.38 angstrom resolution with three molecules in the asymmetric unit. It may provide a structural basis for functional analysis of choline-binding proteins.
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